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P35556

- FBN2_HUMAN

UniProt

P35556 - FBN2_HUMAN

Protein

Fibrillin-2

Gene

FBN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (26 May 2009)
      Previous versions | rss
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    Functioni

    Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. extracellular matrix structural constituent Source: ProtInc

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. bone trabecula formation Source: BHF-UCL
    3. embryonic limb morphogenesis Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. positive regulation of bone mineralization Source: BHF-UCL
    7. positive regulation of osteoblast differentiation Source: BHF-UCL
    8. sequestering of TGFbeta in extracellular matrix Source: BHF-UCL

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibrillin-2
    Gene namesi
    Name:FBN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:3604. FBN2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. microfibril Source: BHF-UCL
    3. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Arthrogryposis, distal, 9 (DA9) [MIM:121050]: A form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti391 – 3911E → K in DA9.
    VAR_015851
    Natural varianti754 – 7541G → S in DA9. 1 Publication
    VAR_058364
    Natural varianti1057 – 10571G → D in DA9. 2 Publications
    VAR_054981
    Natural varianti1091 – 10911N → S in DA9. 1 Publication
    VAR_058365
    Natural varianti1093 – 10931I → T in DA9. 2 Publications
    VAR_054982
    Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
    VAR_010739
    Natural varianti1122 – 11221S → P in DA9. 1 Publication
    VAR_058366
    Natural varianti1142 – 11421C → F in DA9. 2 Publications
    VAR_010740
    Natural varianti1142 – 11421C → R in DA9. 1 Publication
    VAR_058367
    Natural varianti1146 – 11461Y → C in DA9. 1 Publication
    VAR_058368
    Natural varianti1156 – 11561C → F in DA9. 1 Publication
    VAR_058369
    Natural varianti1161 – 11611E → K in DA9. 1 Publication
    VAR_058370
    Natural varianti1179 – 11791G → C in DA9. 1 Publication
    VAR_054983
    Natural varianti1198 – 11981C → Y in DA9. 1 Publication
    VAR_054984
    Natural varianti1240 – 12401C → R in DA9. 1 Publication
    VAR_054985
    Natural varianti1246 – 12461C → F in DA9. 1 Publication
    VAR_058371
    Natural varianti1253 – 12531C → W in DA9. 2 Publications
    Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
    VAR_010741
    Natural varianti1253 – 12531C → Y in DA9. 2 Publications
    VAR_002350
    Natural varianti1257 – 12571C → W in DA9. 1 Publication
    VAR_054986
    Natural varianti1268 – 12681C → R in DA9. 1 Publication
    VAR_054987
    Natural varianti1384 – 13841C → F in DA9. 1 Publication
    VAR_058372
    Natural varianti1384 – 13841C → Y in DA9. 1 Publication
    VAR_058373
    Natural varianti1408 – 14081D → N in DA9. 1 Publication
    VAR_058374
    Natural varianti1425 – 14251C → R in DA9. 1 Publication
    VAR_058375
    Natural varianti1434 – 14341C → S in DA9. 2 Publications
    VAR_002351

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi121050. phenotype.
    Orphaneti115. Congenital contractural arachnodactyly.
    PharmGKBiPA28017.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 29122884Fibrillin-2PRO_0000007584Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi115 ↔ 124PROSITE-ProRule annotation
    Disulfide bondi119 ↔ 130PROSITE-ProRule annotation
    Disulfide bondi132 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi149 ↔ 159PROSITE-ProRule annotation
    Disulfide bondi153 ↔ 164PROSITE-ProRule annotation
    Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
    Disulfide bondi180 ↔ 190PROSITE-ProRule annotation
    Disulfide bondi184 ↔ 196PROSITE-ProRule annotation
    Disulfide bondi198 ↔ 207PROSITE-ProRule annotation
    Disulfide bondi280 ↔ 292PROSITE-ProRule annotation
    Disulfide bondi287 ↔ 301PROSITE-ProRule annotation
    Disulfide bondi303 ↔ 316PROSITE-ProRule annotation
    Disulfide bondi322 ↔ 334PROSITE-ProRule annotation
    Disulfide bondi329 ↔ 343PROSITE-ProRule annotation
    Disulfide bondi345 ↔ 358PROSITE-ProRule annotation
    Glycosylationi492 – 4921N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi498 ↔ 510PROSITE-ProRule annotation
    Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
    Disulfide bondi521 ↔ 533PROSITE-ProRule annotation
    Disulfide bondi539 ↔ 549PROSITE-ProRule annotation
    Disulfide bondi544 ↔ 558PROSITE-ProRule annotation
    Disulfide bondi560 ↔ 573PROSITE-ProRule annotation
    Disulfide bondi579 ↔ 591PROSITE-ProRule annotation
    Disulfide bondi586 ↔ 600PROSITE-ProRule annotation
    Disulfide bondi602 ↔ 615PROSITE-ProRule annotation
    Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
    Disulfide bondi627 ↔ 641PROSITE-ProRule annotation
    Disulfide bondi643 ↔ 656PROSITE-ProRule annotation
    Disulfide bondi662 ↔ 673PROSITE-ProRule annotation
    Disulfide bondi668 ↔ 682PROSITE-ProRule annotation
    Disulfide bondi684 ↔ 697PROSITE-ProRule annotation
    Disulfide bondi772 ↔ 784PROSITE-ProRule annotation
    Disulfide bondi779 ↔ 793PROSITE-ProRule annotation
    Disulfide bondi795 ↔ 808PROSITE-ProRule annotation
    Disulfide bondi814 ↔ 826PROSITE-ProRule annotation
    Disulfide bondi821 ↔ 835PROSITE-ProRule annotation
    Disulfide bondi837 ↔ 850PROSITE-ProRule annotation
    Disulfide bondi856 ↔ 866PROSITE-ProRule annotation
    Disulfide bondi861 ↔ 875PROSITE-ProRule annotation
    Disulfide bondi877 ↔ 890PROSITE-ProRule annotation
    Disulfide bondi959 ↔ 971PROSITE-ProRule annotation
    Disulfide bondi966 ↔ 980PROSITE-ProRule annotation
    Disulfide bondi982 ↔ 995PROSITE-ProRule annotation
    Disulfide bondi1077 ↔ 1089PROSITE-ProRule annotation
    Disulfide bondi1084 ↔ 1098PROSITE-ProRule annotation
    Disulfide bondi1100 ↔ 1113PROSITE-ProRule annotation
    Glycosylationi1112 – 11121N-linked (GlcNAc...)1 Publication
    Disulfide bondi1119 ↔ 1131PROSITE-ProRule annotation
    Disulfide bondi1126 ↔ 1140PROSITE-ProRule annotation
    Disulfide bondi1142 ↔ 1156PROSITE-ProRule annotation
    Disulfide bondi1162 ↔ 1174PROSITE-ProRule annotation
    Disulfide bondi1169 ↔ 1183PROSITE-ProRule annotation
    Disulfide bondi1185 ↔ 1198PROSITE-ProRule annotation
    Disulfide bondi1204 ↔ 1216PROSITE-ProRule annotation
    Disulfide bondi1211 ↔ 1225PROSITE-ProRule annotation
    Disulfide bondi1227 ↔ 1240PROSITE-ProRule annotation
    Disulfide bondi1246 ↔ 1257PROSITE-ProRule annotation
    Disulfide bondi1253 ↔ 1266PROSITE-ProRule annotation
    Disulfide bondi1268 ↔ 1281PROSITE-ProRule annotation
    Disulfide bondi1287 ↔ 1299PROSITE-ProRule annotation
    Disulfide bondi1294 ↔ 1308PROSITE-ProRule annotation
    Disulfide bondi1310 ↔ 1323PROSITE-ProRule annotation
    Disulfide bondi1329 ↔ 1341PROSITE-ProRule annotation
    Disulfide bondi1336 ↔ 1350PROSITE-ProRule annotation
    Disulfide bondi1352 ↔ 1365PROSITE-ProRule annotation
    Disulfide bondi1371 ↔ 1384PROSITE-ProRule annotation
    Disulfide bondi1378 ↔ 1393PROSITE-ProRule annotation
    Disulfide bondi1395 ↔ 1406PROSITE-ProRule annotation
    Disulfide bondi1412 ↔ 1425PROSITE-ProRule annotation
    Glycosylationi1414 – 14141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1419 ↔ 1434PROSITE-ProRule annotation
    Disulfide bondi1436 ↔ 1447PROSITE-ProRule annotation
    Disulfide bondi1453 ↔ 1465PROSITE-ProRule annotation
    Disulfide bondi1460 ↔ 1474PROSITE-ProRule annotation
    Disulfide bondi1476 ↔ 1489PROSITE-ProRule annotation
    Disulfide bondi1495 ↔ 1506PROSITE-ProRule annotation
    Disulfide bondi1501 ↔ 1515PROSITE-ProRule annotation
    Disulfide bondi1517 ↔ 1530PROSITE-ProRule annotation
    Glycosylationi1529 – 15291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1536 ↔ 1547PROSITE-ProRule annotation
    Disulfide bondi1542 ↔ 1556PROSITE-ProRule annotation
    Disulfide bondi1558 ↔ 1571PROSITE-ProRule annotation
    Glycosylationi1625 – 16251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1654 ↔ 1666PROSITE-ProRule annotation
    Disulfide bondi1661 ↔ 1675PROSITE-ProRule annotation
    Disulfide bondi1677 ↔ 1690PROSITE-ProRule annotation
    Disulfide bondi1696 ↔ 1708PROSITE-ProRule annotation
    Disulfide bondi1703 ↔ 1717PROSITE-ProRule annotation
    Glycosylationi1714 – 17141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1719 ↔ 1732PROSITE-ProRule annotation
    Glycosylationi1745 – 17451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1756 – 17561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1812 ↔ 1824PROSITE-ProRule annotation
    Disulfide bondi1819 ↔ 1833PROSITE-ProRule annotation
    Disulfide bondi1835 ↔ 1848PROSITE-ProRule annotation
    Disulfide bondi1854 ↔ 1867PROSITE-ProRule annotation
    Disulfide bondi1861 ↔ 1876PROSITE-ProRule annotation
    Disulfide bondi1878 ↔ 1890PROSITE-ProRule annotation
    Disulfide bondi1896 ↔ 1908PROSITE-ProRule annotation
    Disulfide bondi1903 ↔ 1917PROSITE-ProRule annotation
    Disulfide bondi1919 ↔ 1932PROSITE-ProRule annotation
    Disulfide bondi1938 ↔ 1948PROSITE-ProRule annotation
    Disulfide bondi1943 ↔ 1957PROSITE-ProRule annotation
    Glycosylationi1945 – 19451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1959 ↔ 1971PROSITE-ProRule annotation
    Disulfide bondi1977 ↔ 1990PROSITE-ProRule annotation
    Disulfide bondi1985 ↔ 1999PROSITE-ProRule annotation
    Disulfide bondi2001 ↔ 2014PROSITE-ProRule annotation
    Disulfide bondi2020 ↔ 2032PROSITE-ProRule annotation
    Disulfide bondi2027 ↔ 2041PROSITE-ProRule annotation
    Disulfide bondi2043 ↔ 2054PROSITE-ProRule annotation
    Disulfide bondi2060 ↔ 2072PROSITE-ProRule annotation
    Disulfide bondi2067 ↔ 2081PROSITE-ProRule annotation
    Disulfide bondi2083 ↔ 2096PROSITE-ProRule annotation
    Glycosylationi2120 – 21201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2175 ↔ 2187PROSITE-ProRule annotation
    Disulfide bondi2182 ↔ 2196PROSITE-ProRule annotation
    Disulfide bondi2198 ↔ 2211PROSITE-ProRule annotation
    Disulfide bondi2217 ↔ 2228PROSITE-ProRule annotation
    Disulfide bondi2223 ↔ 2237PROSITE-ProRule annotation
    Glycosylationi2225 – 22251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2239 ↔ 2251PROSITE-ProRule annotation
    Disulfide bondi2257 ↔ 2268PROSITE-ProRule annotation
    Disulfide bondi2264 ↔ 2277PROSITE-ProRule annotation
    Disulfide bondi2279 ↔ 2292PROSITE-ProRule annotation
    Disulfide bondi2298 ↔ 2312PROSITE-ProRule annotation
    Disulfide bondi2305 ↔ 2321PROSITE-ProRule annotation
    Disulfide bondi2323 ↔ 2336PROSITE-ProRule annotation
    Disulfide bondi2342 ↔ 2354PROSITE-ProRule annotation
    Disulfide bondi2349 ↔ 2363PROSITE-ProRule annotation
    Disulfide bondi2365 ↔ 2378PROSITE-ProRule annotation
    Disulfide bondi2453 ↔ 2465PROSITE-ProRule annotation
    Disulfide bondi2460 ↔ 2474PROSITE-ProRule annotation
    Disulfide bondi2476 ↔ 2489PROSITE-ProRule annotation
    Disulfide bondi2495 ↔ 2506PROSITE-ProRule annotation
    Disulfide bondi2502 ↔ 2515PROSITE-ProRule annotation
    Disulfide bondi2517 ↔ 2530PROSITE-ProRule annotation
    Disulfide bondi2536 ↔ 2547PROSITE-ProRule annotation
    Disulfide bondi2543 ↔ 2556PROSITE-ProRule annotation
    Disulfide bondi2558 ↔ 2569PROSITE-ProRule annotation
    Disulfide bondi2575 ↔ 2588PROSITE-ProRule annotation
    Disulfide bondi2582 ↔ 2597PROSITE-ProRule annotation
    Disulfide bondi2599 ↔ 2612PROSITE-ProRule annotation
    Disulfide bondi2618 ↔ 2628PROSITE-ProRule annotation
    Disulfide bondi2624 ↔ 2637PROSITE-ProRule annotation
    Disulfide bondi2639 ↔ 2652PROSITE-ProRule annotation
    Disulfide bondi2658 ↔ 2669PROSITE-ProRule annotation
    Disulfide bondi2664 ↔ 2678PROSITE-ProRule annotation
    Disulfide bondi2680 ↔ 2693PROSITE-ProRule annotation
    Disulfide bondi2699 ↔ 2710PROSITE-ProRule annotation
    Disulfide bondi2706 ↔ 2719PROSITE-ProRule annotation
    Disulfide bondi2721 ↔ 2733PROSITE-ProRule annotation
    Glycosylationi2808 – 28081N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP35556.
    PaxDbiP35556.
    PRIDEiP35556.

    PTM databases

    PhosphoSiteiP35556.

    Expressioni

    Gene expression databases

    ArrayExpressiP35556.
    BgeeiP35556.
    CleanExiHS_FBN2.
    GenevestigatoriP35556.

    Organism-specific databases

    HPAiCAB026401.
    HPA012853.

    Interactioni

    Protein-protein interaction databases

    BioGridi108495. 7 interactions.
    IntActiP35556. 3 interactions.
    STRINGi9606.ENSP00000262464.

    Structurei

    3D structure databases

    ProteinModelPortaliP35556.
    SMRiP35556. Positions 75-996, 1073-2330, 2338-2721.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 14232EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 17632EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini176 – 20833EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini214 – 26653TB 1Add
    BLAST
    Domaini276 – 31742EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini318 – 35942EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 41754TB 2Add
    BLAST
    Domaini494 – 53441EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini535 – 57440EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini575 – 61642EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini617 – 65741EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini658 – 69841EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini704 – 75653TB 3Add
    BLAST
    Domaini768 – 80942EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini810 – 85142EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini852 – 89140EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini896 – 94752TB 4Add
    BLAST
    Domaini955 – 99642EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1001 – 105252TB 5Add
    BLAST
    Domaini1073 – 111442EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1115 – 115743EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1158 – 119942EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1200 – 124142EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1242 – 128241EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1283 – 132442EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1325 – 136642EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1367 – 140741EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1408 – 144841EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1449 – 149042EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1491 – 153141EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1532 – 157241EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1577 – 163357TB 6Add
    BLAST
    Domaini1650 – 169142EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1692 – 173342EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1738 – 179154TB 7Add
    BLAST
    Domaini1808 – 184942EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1850 – 189142EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1892 – 193342EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1934 – 197239EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1973 – 201543EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2016 – 205540EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2056 – 209742EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2102 – 215554TB 8Add
    BLAST
    Domaini2171 – 221242EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2213 – 225240EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2253 – 229341EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2294 – 233744EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2338 – 237942EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2384 – 243754TB 9Add
    BLAST
    Domaini2449 – 249042EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2491 – 253141EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2532 – 257039EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2571 – 261343EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2614 – 265340EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2654 – 269441EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2695 – 273440EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fibrillin family.Curated
    Contains 47 EGF-like domains.PROSITE-ProRule annotation
    Contains 9 TB (TGF-beta binding) domains.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231768.
    HOVERGENiHBG005643.
    InParanoidiP35556.
    OMAiSGRNCID.
    OrthoDBiEOG7RV9F6.
    PhylomeDBiP35556.
    TreeFamiTF316849.

    Family and domain databases

    Gene3Di3.90.290.10. 9 hits.
    InterProiIPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR011398. FBN/EtMIC4.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view]
    PANTHERiPTHR24039. PTHR24039. 1 hit.
    PfamiPF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 41 hits.
    PF00683. TB. 9 hits.
    [Graphical view]
    PIRSFiPIRSF036312. Fibrillin. 1 hit.
    SMARTiSM00181. EGF. 3 hits.
    SM00179. EGF_CA. 43 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 13 hits.
    SSF57581. SSF57581. 9 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 37 hits.
    PS50026. EGF_3. 45 hits.
    PS01187. EGF_CA. 43 hits.
    PS51364. TB. 9 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35556-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA     50
    TAGSEGGFLA PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG 100
    WKTLPGGNQC IVPICRNSCG DGFCSRPNMC TCSSGQISST CGSKSIQQCS 150
    VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC ENGCQNGGRC IGPNRCACVY 200
    GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC ATIGRAWGHP 250
    CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE 300
    CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV 350
    TSTDGSRCID QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT 400
    IPEACPVRGS EEYRRLCMDG LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG 450
    YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG QGPIITGLTI LNQTIDICKH 500
    HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT SNPCTNGDCV 550
    NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC 600
    ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA 650
    PNGRYCTDVD ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT 700
    HMRSTCYGGI KKGVCVRPFP GAVTKSECCC ANPDYGFGEP CQPCPAKNSA 750
    EFHGLCSSGV GITVDGRDIN ECALDPDICA NGICENLRGS YRCNCNSGYE 800
    PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG YVFRTETETC 850
    EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL 900
    NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG 950
    VTCEDVNECE VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM 1000
    EQCYLKWDED ECIHPVPGKF RMDACCCAVG AAWGTECEEC PKPGTKEYET 1050
    LCPRGAGFAN RGDVLTGRPF YKDINECKAF PGMCTYGKCR NTIGSFKCRC 1100
    NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC ECFEGYESGF 1150
    MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD 1200
    INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN 1250
    GGCDTQCTNS EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT 1300
    NIPGEYRCLC YDGFMASMDM KTCIDVNECD LNSNICMFGE CENTKGSFIC 1350
    HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM HASCLNIPGS FKCSCREGWI 1400
    GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF TGDGFTCSDV 1450
    DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI 1500
    CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT 1550
    PGRYECNCPP DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG 1600
    VSRSSCCCSL GKAWGNPCET CPPVNSTEYY TLCPGGEGFR PNPITIILED 1650
    IDECQELPGL CQGGNCINTF GSFQCECPQG YYLSEDTRIC EDIDECFAHP 1700
    GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC YRSYNGTTCE 1750
    NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD 1800
    IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED 1850
    IDECSNGDNL CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP 1900
    NVCSHGLCVD LQGSYQCICH NGFKASQDQT MCMDVDECER HPCGNGTCKN 1950
    TVGSYNCLCY PGFELTHNND CLDIDECSSF FGQVCRNGRC FNEIGSFKCL 2000
    CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR CICPPGYEVK 2050
    SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR 2100
    QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA 2150
    FQDLCPYGHG TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM 2200
    GYNLDYTGVR CVDTDECSIG NPCGNGTCTN VIGSFECNCN EGFEPGPMMN 2250
    CEDINECAQN PLLCAFRCMN TFGSYECTCP IGYALREDQK MCKDLDECAE 2300
    GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN ECRTKPGICE 2350
    NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS 2400
    SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI 2450
    DECKVMPNLC TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK 2500
    PCNYICKNTE GSYQCSCPRG YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT 2550
    LGGFTCKCPP GFTQHHTACI DNNECGSQPS LCGAKGICQN TPGSFSCECQ 2600
    RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP QGYIQHYQWN 2650
    QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS 2700
    SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE 2750
    VDEENALSPE ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD 2800
    SPVNMKFNLS HLGSKEHILE LRPAIQPLNN HIRYVISQGN DDSVFRIHQR 2850
    NGLSYLHTAK KKLMPGTYTL EITSIPLYKK KELKKLEESN EDDYLLGELG 2900
    EALRMRLQIQ LY 2912
    Length:2,912
    Mass (Da):314,775
    Last modified:May 26, 2009 - v3
    Checksum:i0F0D78319E9911E6
    GO
    Isoform 2 (identifier: P35556-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         113-145: Missing.
         1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
         1507-2912: Missing.

    Show »
    Length:1,473
    Mass (Da):157,690
    Checksum:i2B6620CFCA6F7A72
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti146 – 1461I → L in BAG62163. (PubMed:14702039)Curated
    Sequence conflicti192 – 1954GPNR → AQP in AAA18950. (PubMed:8120105)Curated
    Sequence conflicti243 – 2431I → T in AAA18950. (PubMed:8120105)Curated
    Sequence conflicti243 – 2431I → T in BAG62163. (PubMed:14702039)Curated
    Sequence conflicti1161 – 11611E → G in AAA18950. (PubMed:8120105)Curated
    Sequence conflicti1161 – 11611E → G in CAB56757. (PubMed:1852206)Curated
    Sequence conflicti1244 – 12441D → G in BAG62163. (PubMed:14702039)Curated
    Sequence conflicti1409 – 14091L → R in CAB56757. (PubMed:1852206)Curated
    Sequence conflicti1503 – 15031F → S in AAA18950. (PubMed:8120105)Curated
    Sequence conflicti2584 – 25841A → G in AAA18950. (PubMed:8120105)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti391 – 3911E → K in DA9.
    VAR_015851
    Natural varianti594 – 5941T → S.2 Publications
    VAR_054979
    Natural varianti681 – 6811R → H.1 Publication
    VAR_054980
    Natural varianti754 – 7541G → S in DA9. 1 Publication
    VAR_058364
    Natural varianti965 – 9651V → I.3 Publications
    Corresponds to variant rs154001 [ dbSNP | Ensembl ].
    VAR_002349
    Natural varianti1057 – 10571G → D in DA9. 2 Publications
    VAR_054981
    Natural varianti1091 – 10911N → S in DA9. 1 Publication
    VAR_058365
    Natural varianti1093 – 10931I → T in DA9. 2 Publications
    VAR_054982
    Natural varianti1115 – 11151D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 Publications
    VAR_010739
    Natural varianti1122 – 11221S → P in DA9. 1 Publication
    VAR_058366
    Natural varianti1142 – 11421C → F in DA9. 2 Publications
    VAR_010740
    Natural varianti1142 – 11421C → R in DA9. 1 Publication
    VAR_058367
    Natural varianti1146 – 11461Y → C in DA9. 1 Publication
    VAR_058368
    Natural varianti1156 – 11561C → F in DA9. 1 Publication
    VAR_058369
    Natural varianti1161 – 11611E → K in DA9. 1 Publication
    VAR_058370
    Natural varianti1179 – 11791G → C in DA9. 1 Publication
    VAR_054983
    Natural varianti1198 – 11981C → Y in DA9. 1 Publication
    VAR_054984
    Natural varianti1240 – 12401C → R in DA9. 1 Publication
    VAR_054985
    Natural varianti1246 – 12461C → F in DA9. 1 Publication
    VAR_058371
    Natural varianti1253 – 12531C → W in DA9. 2 Publications
    Corresponds to variant rs28931602 [ dbSNP | Ensembl ].
    VAR_010741
    Natural varianti1253 – 12531C → Y in DA9. 2 Publications
    VAR_002350
    Natural varianti1257 – 12571C → W in DA9. 1 Publication
    VAR_054986
    Natural varianti1268 – 12681C → R in DA9. 1 Publication
    VAR_054987
    Natural varianti1384 – 13841C → F in DA9. 1 Publication
    VAR_058372
    Natural varianti1384 – 13841C → Y in DA9. 1 Publication
    VAR_058373
    Natural varianti1408 – 14081D → N in DA9. 1 Publication
    VAR_058374
    Natural varianti1425 – 14251C → R in DA9. 1 Publication
    VAR_058375
    Natural varianti1434 – 14341C → S in DA9. 2 Publications
    VAR_002351
    Natural varianti1772 – 17721W → G.2 Publications
    VAR_054988
    Natural varianti2062 – 20621E → V Found in a renal cell carcinoma case; somatic mutation. 1 Publication
    VAR_064705
    Natural varianti2266 – 22661F → L.2 Publications
    VAR_054989
    Natural varianti2278 – 22781T → M.
    Corresponds to variant rs2307109 [ dbSNP | Ensembl ].
    VAR_055415
    Natural varianti2311 – 23111M → V.
    Corresponds to variant rs32209 [ dbSNP | Ensembl ].
    VAR_055416
    Natural varianti2428 – 24281P → T.1 Publication
    Corresponds to variant rs1801169 [ dbSNP | Ensembl ].
    VAR_016143
    Natural varianti2580 – 25801S → L.1 Publication
    Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
    VAR_055417
    Natural varianti2581 – 25811L → S.
    Corresponds to variant rs2291628 [ dbSNP | Ensembl ].
    VAR_054990
    Natural varianti2771 – 27711S → P.2 Publications
    Corresponds to variant rs1801170 [ dbSNP | Ensembl ].
    VAR_014664

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei113 – 14533Missing in isoform 2. 2 PublicationsVSP_037369Add
    BLAST
    Alternative sequencei1491 – 150616DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2. 2 PublicationsVSP_037370Add
    BLAST
    Alternative sequencei1507 – 29121406Missing in isoform 2. 2 PublicationsVSP_037371Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03272 mRNA. Translation: AAA18950.1.
    AK300440 mRNA. Translation: BAG62163.1.
    AC025169 Genomic DNA. No translation available.
    AC034235 Genomic DNA. No translation available.
    AC113387 Genomic DNA. No translation available.
    X62009 mRNA. Translation: CAB56757.1.
    AB209735 mRNA. Translation: BAD92972.1.
    CCDSiCCDS34222.1. [P35556-1]
    PIRiA54105.
    RefSeqiNP_001990.2. NM_001999.3. [P35556-1]
    UniGeneiHs.519294.

    Genome annotation databases

    EnsembliENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
    ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
    GeneIDi2201.
    KEGGihsa:2201.
    UCSCiuc003kuu.3. human. [P35556-1]

    Polymorphism databases

    DMDMi238054385.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03272 mRNA. Translation: AAA18950.1 .
    AK300440 mRNA. Translation: BAG62163.1 .
    AC025169 Genomic DNA. No translation available.
    AC034235 Genomic DNA. No translation available.
    AC113387 Genomic DNA. No translation available.
    X62009 mRNA. Translation: CAB56757.1 .
    AB209735 mRNA. Translation: BAD92972.1 .
    CCDSi CCDS34222.1. [P35556-1 ]
    PIRi A54105.
    RefSeqi NP_001990.2. NM_001999.3. [P35556-1 ]
    UniGenei Hs.519294.

    3D structure databases

    ProteinModelPortali P35556.
    SMRi P35556. Positions 75-996, 1073-2330, 2338-2721.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108495. 7 interactions.
    IntActi P35556. 3 interactions.
    STRINGi 9606.ENSP00000262464.

    PTM databases

    PhosphoSitei P35556.

    Polymorphism databases

    DMDMi 238054385.

    Proteomic databases

    MaxQBi P35556.
    PaxDbi P35556.
    PRIDEi P35556.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262464 ; ENSP00000262464 ; ENSG00000138829 . [P35556-1 ]
    ENST00000508053 ; ENSP00000424571 ; ENSG00000138829 . [P35556-1 ]
    GeneIDi 2201.
    KEGGi hsa:2201.
    UCSCi uc003kuu.3. human. [P35556-1 ]

    Organism-specific databases

    CTDi 2201.
    GeneCardsi GC05M127621.
    GeneReviewsi FBN2.
    H-InvDB HIX0005141.
    HIX0137461.
    HGNCi HGNC:3604. FBN2.
    HPAi CAB026401.
    HPA012853.
    MIMi 121050. phenotype.
    612570. gene.
    neXtProti NX_P35556.
    Orphaneti 115. Congenital contractural arachnodactyly.
    PharmGKBi PA28017.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231768.
    HOVERGENi HBG005643.
    InParanoidi P35556.
    OMAi SGRNCID.
    OrthoDBi EOG7RV9F6.
    PhylomeDBi P35556.
    TreeFami TF316849.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.

    Miscellaneous databases

    GenomeRNAii 2201.
    NextBioi 8895.
    PROi P35556.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35556.
    Bgeei P35556.
    CleanExi HS_FBN2.
    Genevestigatori P35556.

    Family and domain databases

    Gene3Di 3.90.290.10. 9 hits.
    InterProi IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR011398. FBN/EtMIC4.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view ]
    PANTHERi PTHR24039. PTHR24039. 1 hit.
    Pfami PF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 41 hits.
    PF00683. TB. 9 hits.
    [Graphical view ]
    PIRSFi PIRSF036312. Fibrillin. 1 hit.
    SMARTi SM00181. EGF. 3 hits.
    SM00179. EGF_CA. 43 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 13 hits.
    SSF57581. SSF57581. 9 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 43 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 37 hits.
    PS50026. EGF_3. 45 hits.
    PS01187. EGF_CA. 43 hits.
    PS51364. TB. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices."
      Zhang H., Apfelroth S.D., Hu W., Davis E.C., Sanguineti C., Bonadio J., Mecham R.P., Ramirez F.
      J. Cell Biol. 124:855-863(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-594; GLY-1772; LEU-2266; LEU-2580 AND PRO-2771.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Placenta.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Linkage of Marfan syndrome and a phenotypically related disorder to two different fibrillin genes."
      Lee B., Godfrey M., Vitale E., Hori H., Mattei M.-G., Sarfarazi M., Tsipouras P., Ramirez F., Hollister D.W.
      Nature 352:330-334(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 752-2912 (ISOFORM 2).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 937-2912 (ISOFORM 1).
      Tissue: Aortic endothelium.
    6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1112.
      Tissue: Liver.
    7. "Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly."
      Putnam E.A., Zhang H., Ramirez F., Milewicz D.M.
      Nat. Genet. 11:456-458(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DA9 TYR-1253 AND SER-1434, VARIANT ILE-965.
    8. "Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development."
      Park E.-S., Putnam E.A., Chitayat D., Child A., Milewicz D.M.
      Am. J. Med. Genet. 78:350-355(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DA9 ASP-1057 AND THR-1093, VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771.
    9. "A single mutation that results in an Asp-to-His substitution and partial exon skipping in a family with congenital contractural arachnodactyly."
      Babcock D., Gasner C., Francke U., Maslen C.
      Hum. Genet. 103:22-28(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DA9 HIS-1115.
    10. "Two novel fibrillin-2 mutations in congenital contractural arachnodactyly."
      Belleh S., Zhou G., Wang M., Der Kaloustian V.M., Pagon R.A., Godfrey M.
      Am. J. Med. Genet. 92:7-12(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DA9 PHE-1142 AND TRP-1253.
    11. "Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype."
      Gupta P.A., Putnam E.A., Carmical S.G., Kaitila I., Steinmann B., Child A., Danesino C., Metcalfe K., Berry S.A., Chen E., Delorme C.V., Thong M.-K., Ades L.C., Milewicz D.M.
      Hum. Mutat. 19:39-48(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DA9 ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434, VARIANT ILE-965.
    12. "Comprehensive clinical and molecular assessment of 32 probands with congenital contractural arachnodactyly: report of 14 novel mutations and review of the literature."
      Callewaert B.L., Loeys B.L., Ficcadenti A., Vermeer S., Landgren M., Kroes H.Y., Yaron Y., Pope M., Foulds N., Boute O., Galan F., Kingston H., Van der Aa N., Salcedo I., Swinkels M.E., Wallgren-Pettersson C., Gabrielli O., De Backer J., Coucke P.J., De Paepe A.M.
      Hum. Mutat. 30:334-341(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS DA9 SER-754; SER-1091; HIS-1115; PRO-1122; ARG-1142; CYS-1146; PHE-1156; LYS-1161; PHE-1246; PHE-1384; TYR-1384; ASN-1408 AND ARG-1425.
    13. Cited for: VARIANT VAL-2062.

    Entry informationi

    Entry nameiFBN2_HUMAN
    AccessioniPrimary (citable) accession number: P35556
    Secondary accession number(s): B4DU01, Q59ES6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 157 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3